SRC_AVISR
ID SRC_AVISR Reviewed; 526 AA.
AC P00525;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Tyrosine-protein kinase transforming protein Src;
DE EC=2.7.10.2;
DE AltName: Full=pp60v-src;
DE Short=p60-Src;
DE Short=v-Src;
GN Name=V-SRC;
OS Avian sarcoma virus (strain rASV1441).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus;
OC unclassified Alpharetrovirus.
OX NCBI_TaxID=11894;
OH NCBI_TaxID=8976; Galliformes.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6292477; DOI=10.1128/jvi.44.1.1-11.1982;
RA Takeya T., Feldman R.A., Hanafusa H.;
RT "DNA sequence of the viral and cellular src gene of chickens. 1. Complete
RT nucleotide sequence of an EcoRI fragment of recovered avian sarcoma virus
RT which codes for gp37 and pp60src.";
RL J. Virol. 44:1-11(1982).
RN [2]
RP PHOSPHORYLATION AT TYR-416.
RX PubMed=6264320; DOI=10.1038/291675a0;
RA Neil J.C., Ghysdael J., Vogt P.K., Smart J.E.;
RT "Homologous tyrosine phosphorylation sites in transformation-specific gene
RT products of distinct avian sarcoma viruses.";
RL Nature 291:675-677(1981).
RN [3]
RP STRUCTURE BY NMR OF 85-140.
RX PubMed=7526465; DOI=10.1126/science.7526465;
RA Feng S., Chen J.K., Yu H., Simon J.A., Schreiber S.L.;
RT "Two binding orientations for peptides to the Src SH3 domain: development
RT of a general model for SH3-ligand interactions.";
RL Science 266:1241-1247(1994).
CC -!- FUNCTION: This phosphoprotein, required for both the initiation and the
CC maintenance of neoplastic transformation, is a protein kinase that
CC catalyzes the phosphorylation of tyrosine residues in vitro.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- PTM: The phosphorylated form is termed pp60v-src.
CC {ECO:0000269|PubMed:6264320}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. SRC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; K00928; AAA42565.1; -; Genomic_RNA.
DR PDB; 1QWE; NMR; -; A=81-140.
DR PDB; 1QWF; NMR; -; A=81-140.
DR PDBsum; 1QWE; -.
DR PDBsum; 1QWF; -.
DR BMRB; P00525; -.
DR SMR; P00525; -.
DR BindingDB; P00525; -.
DR iPTMnet; P00525; -.
DR BRENDA; 2.7.10.2; 600.
DR EvolutionaryTrace; P00525; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Lipoprotein; Myristate;
KW Nucleotide-binding; Oncogene; Phosphoprotein; SH2 domain; SH3 domain;
KW Transferase; Tyrosine-protein kinase.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250"
FT CHAIN 2..526
FT /note="Tyrosine-protein kinase transforming protein Src"
FT /id="PRO_0000088147"
FT DOMAIN 81..142
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 148..245
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 267..517
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 386
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 273..281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 416
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:6264320"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:1QWE"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:1QWE"
FT STRAND 114..123
FT /evidence="ECO:0007829|PDB:1QWE"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:1QWE"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:1QWE"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:1QWE"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:1QWE"
SQ SEQUENCE 526 AA; 58878 MW; 7DB3903F80233E49 CRC64;
MGSSKSKPKD PSQRRCSLEP PDSTHHGGFP ASQTPNKTAA PDTHRTPSRS FGTVATEPKL
FGGFNTSDTV TSPQRAGALA GGVTTFVALY DYESRTETDL SFKKGERLQI VNNTEGDWWL
AHSLTTGQTG YIPSNYVAPS DSIQAEEWYF GKITRRESER LLLNPENPRG TFLVRESETT
KGAYCLSVSD FDNAKGLNVK HYKIRKLDSG GFYITSRTQF SSLQQLVAYY SKHADGLCHR
LTNVCPTSKP QTQGLAKDAW EIPRESLRLE VKLGQGCFGE VWMGTWNGTT RVAIKTLKPG
TMSPEAFLQE AQVMKKLRHE KLVQLYAVVS EEPIYIVTEY MSKGSLLDFL KGEMGKYLRL
PQLVDMAAQI ASGMAYVERM NYVHRDLRAA NILVGENLVC KVADFGLARL IEDNEYTARQ
GAKFPIKWTA PEAALYGRFT IKSDVWSFGI LLTELTTKGR VPYPGMGNGE VLDRVERGYR
MPCPPECPES LHDLMCQCWR RDPEERPTFE YLQAQLLPAC VLEVAE
